RH2_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RH2_ARATH
• UniProt AC: Q94A52
• Protein Name: Eukaryotic initiation factor 4A-III homolog {ECO:0000305}
• Gene Name: EIF4A3 {ECO:0000303|PubMed:19435936}
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 408
• Subcellular Localization: Nucleus, nucleoplasm . Nucleus, nucleolus . Nucleus speckle . Nucleus . Cytoplasm . Hypoxia causes transition from diffuse nucleoplasmic localization to accumulation in speckles in nuclei of root cells (PubMed:19435936). Localized to the nucleus when
• Protein Description: ATP-dependent RNA helicase. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by MLN51/CASC3, but abolished in presence of the MAGO-Y14 heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGO-Y14 heterodimer increases the RNA-binding affinity of the EJC (By similarity). Plays a role in abiotic stress adaptation. Can regulate abiotic stress resistance partially via the control of acetoacetyl-CoA thiolase 2 (AC Q8S4Y1) expression. [PubMed: 26883227; (Microbial infection) Functions as host RNA helicase that is co-opted by the tombusvirus (TBSV) RNA replication enhancer to greatly enhance tombusvirus replication. Interacts with the viral minus-strand RNA and the replication proteins within the viral replicase.]
• Protein Sequence: MATANPGRGGGRRGGGAMDDDKLVFETTDGIEPITSFNDMGIKEDVLRGVYEYGFEKPSAIQQRAVMPILQGRDVIAQAQSGTGKTSMIALSVCQVVDTSSREVQALILSPTRELATQTEKTIQAIGLHANIQAHACIGGNSVGEDIRKLEHGVHVVSGTPGRVCDMIKRRSLRTRAIKLLILDESDEMLSRGFKDQIYDVYRYLPPDLQVCLVSATLPHEILEMTSKFMTEPVKILVKRDELTLEGIKQFFVAVEKEEWKFDTLCDLYDTLTITQAVIFCNTKRKVDYLSEKMRSHNFTVSSMHGDMPQKERDAIMNEFRSGDSRVLITTDVWARGIDVQQVSLVINYDLPNNRELYIHRIGRSGRFGRKGVAINFVKSDDIKILRDIEQYYSTQIDEMPMNVADLI

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
100	Phosphorylation	VCQVVDTSSREVQAL EEEEECCCCHHHHHH	23.96	26887918
101	Phosphorylation	CQVVDTSSREVQALI EEEECCCCHHHHHHH	34.25	26887918
186	Phosphorylation	KLLILDESDEMLSRG EEEEECCCHHHHHCC	38.24	23820729

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RH2_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
100	S	Phosphorylation	Phosphorylated at Ser-100 and Ser-101.	26887918
100	S	Phosphorylation	Phosphorylation status of Ser-100 and Ser-101 largely determines the subcellular localization of EIF4A3.	26887918
101	S	Phosphorylation	Phosphorylated at Ser-100 and Ser-101.	26887918
101	S	Phosphorylation	Phosphorylation status of Ser-100 and Ser-101 largely determines the subcellular localization of EIF4A3.	26887918

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RH2_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THO4D_ARATH	ALY4	physical	19435936

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.